Dynamics of well-folded and natively disordered proteins in solution: a time-of-flight neutron scattering study
| Autor: | A. M. Gaspar, Wolfgang Doster, Marie-Sousai Appavou, Sebastian Busch, Tobias Unruh |
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| Rok vydání: | 2008 |
| Předmět: |
Protein Folding
Quantitative Biology::Biomolecules Time Factors Hydrodynamic radius Chemistry Scattering Movement Biophysics Caseins General Medicine Neutron scattering Protein Structure Secondary Spectral line Solutions Neutron Diffraction Crystallography Time of flight chemistry.chemical_compound Myoglobin Chemical physics Solvents Cluster (physics) Animals Cattle Structure factor |
| Zdroj: | European Biophysics Journal. 37:573-582 |
| ISSN: | 1432-1017 0175-7571 |
| DOI: | 10.1007/s00249-008-0266-3 |
| Popis: | Casein proteins belong to the class of natively disordered proteins. The existence of disordered biologically active proteins questions the assumption that a well-folded structure is required for function. A hypothesis generally put forward is that the unstructured nature of these proteins results from the functional need of a higher flexibility. This interplay between structure and dynamics was investigated in a series of time-of-flight neutron scattering experiments, performed on casein proteins, as well as on three well-folded proteins with distinct secondary structures, namely, myoglobin (alpha), lysozyme (alpha/beta) and concanavalin A (beta). To illustrate the subtraction of the solvent contribution from the scattering spectra, we used the dynamic susceptibility spectra emphasizing the high frequency part of the spectrum, where the solvent dominates. The quality of the procedure is checked by comparing the corrected spectra to those of the dry and hydrated protein with negligible solvent contamination. Results of spectra analysis reveal differences in motional amplitudes of well-folded proteins, where beta-sheet structures appear to be more rigid than a cluster of alpha-helices. The disordered caseins display the largest conformational displacements. Moreover their global diffusion rates deviate from the expected dependence, suggesting further large-scale conformational motions. |
| Databáze: | OpenAIRE |
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